Copper trafficking to the mitochondrion and assembly of copper metalloenzymes
Autor: | Paul A. Cobine, Dennis R. Winge, Fabien Pierrel |
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Přispěvatelé: | University of Utah, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA) |
Rok vydání: | 2006 |
Předmět: |
Models
Molecular Protein Conformation MESH: Mitochondria Mitochondrial intermembrane space MESH: Biological Transport chemistry.chemical_element macromolecular substances Mitochondrion Cytochrome oxidase Electron Transport Complex IV Superoxide dismutase 03 medical and health sciences MESH: Protein Conformation MESH: Electron Transport Complex IV COX17 Cytochrome c oxidase [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Molecular Biology 030304 developmental biology 0303 health sciences biology Chemistry Metallochaperone 030302 biochemistry & molecular biology nutritional and metabolic diseases Biological Transport Cell Biology Copper Mitochondria MESH: Copper Biochemistry Cytoplasm Mitochondrial matrix Biophysics biology.protein MESH: Models Molecular |
Zdroj: | Biochimica et Biophysica Acta-Molecular Cell Research Biochimica et Biophysica Acta-Molecular Cell Research, Elsevier, 2006, 1763 (7), pp.759-72. ⟨10.1016/j.bbamcr.2006.03.002⟩ Biochimica et Biophysica Acta-Molecular Cell Research, 2006, 1763 (7), pp.759-72. ⟨10.1016/j.bbamcr.2006.03.002⟩ |
ISSN: | 0167-4889 |
DOI: | 10.1016/j.bbamcr.2006.03.002 |
Popis: | International audience; Copper is required within the mitochondrion for the function of two metalloenzymes, cytochrome c oxidase (CcO) and superoxide dismutase (Sod1). Copper metallation of these two enzymes occurs within the mitochondrial intermembrane space and is mediated by metallochaperone proteins. Cox17 is a key copper donor to two accessory proteins, Sco1 and Cox11, to form the two copper centers in the mature CcO complex. Ccs1 is the necessary metallochaperone for the copper metallation of Sod1 in the IMS as well as within the cytoplasm where the bulk of Sod1 resides. Copper ions used in the metallation of CcO and Sod1 appear to be provided by a novel copper pool within the mitochondrial matrix. This review documents copper ion shuttling within the mitochondrion and the proteins that mediate assembly of active CcO and Sod1. |
Databáze: | OpenAIRE |
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